SLU-PP-332

SLU-PP-332 in brief

SLU-PP-332 is a small synthetic acylhydrazone, C18H14N2O2, designed at Saint Louis University in 2023 from the older compound GSK4716 by changing one ring to a naphthalene. It is a laboratory probe that raises the transcriptional output of the three estrogen-related receptors, with its highest reported potency at the alpha paralog in transfected reporter assays. Most of its roughly ten studies come from one group of collaborating laboratories and use cells or animals; there are no human in vivo data. No binding constant has been measured at any of the three receptors and no experimental structure of the molecule exists, so its binding pose is modelled rather than observed.^[1,2,3,4,5]

SLU-PP-332 regulatory status

SLU-PP-332 is not an approved medicine: no marketing authorisation was found in Drugs@FDA, the EMA medicines database or the Health Canada Drug Product Database, and a ClinicalTrials.gov search returns no study with it as an intervention (all searched November 2026). The WADA 2026 Prohibited List does not name it, and it does not name the estrogen-related receptors or their agonists as a class. Section S4.4, metabolic modulators, names activators of AMP-activated protein kinase, peroxisome proliferator-activated receptor delta agonists, Rev-erb agonists, insulins and insulin-mimetics, meldonium and trimetazidine, so estrogen-related receptor agonism is not among the classes that section names. Two other features of the List bear on reading that: its categories are written as including but not limited to their examples, and section S0, non-approved substances, prohibits at all times any pharmacological substance that no other section addresses and that has no current approval by any governmental regulatory health authority for human therapeutic use. It appears neither in the FDA list of bulk drug substances that may present significant safety risks, which therefore records no agency concern against it, nor among the nominations that page lists as withdrawn (checked November 2026), and no retraction or expression of concern was found on any work cited here.^{[6,7,8,9,10,11]}

SLU-PP-332 at a glance

• A small synthetic molecule of 290.3 g/mol, C18H14N2O2, with no stereocentres and an E-configured acylhydrazone linker joining a 4-hydroxyphenyl ring to a naphthalene.^[1]
• Built in 2023 from the older compound GSK4716 by one substituent change, with the explicit aim of reaching the alpha member of the estrogen-related receptor family, which earlier agonists of that chemotype did not activate.^[2,3]
• Not a medicine anywhere and not in clinical study: no marketing authorisation in Drugs@FDA, the EMA medicines database or the Health Canada Drug Product Database, and no registered trial with it as an intervention (searched November 2026). The WADA 2026 Prohibited List names neither the compound nor the receptor family it acts on.^[6,7,8,10,9]
• Reported half-maximal concentrations in a transfected reporter assay of 98 nM at ERRalpha, 230 nM at ERRbeta and 430 nM at ERRgamma in the originating paper, and 0.22 and 0.59 micromolar at the alpha and gamma paralogs in a later paper from an overlapping group. No binding constant has been measured at any of the three.^[2,5]
• No experimental structure of the molecule exists, bound or free. What the molecular picture shows is a calculated conformer, and every published binding pose is a docking or simulation result.^[1,5]
• Two independent doping-control laboratories have characterised it analytically and mapped its in vitro metabolism in human liver preparations, one finding nine metabolites and the other 22.^[12,13]

What is SLU-PP-332?

SLU-PP-332 is a laboratory chemical probe for the estrogen-related receptors, a family of three nuclear receptors named alpha, beta and gamma. A nuclear receptor is a protein that binds DNA and controls transcription of nearby genes; these three share a great deal of sequence with the classical estrogen receptors but do not bind estrogens and have no known natural ligand. They are described as constitutively active, meaning they drive transcription in partnership with a coactivator protein without waiting for a molecule to arrive, and they are concentrated in tissues with heavy oxidative metabolism such as heart, skeletal muscle and liver. Two words used throughout this page are worth fixing here. Paralog means one of several related genes in the same genome that arose by duplication, so alpha, beta and gamma are paralogs of one another rather than one receptor's versions in different species. And every potency figure below is a half-maximal effective concentration, the concentration at which an assay reaches half of its own maximum response, which is a property of the compound in that assay rather than a binding affinity.^[14,15,16]

The compound is older than its pharmacology. It is a plain acylhydrazone that sat in screening catalogues under a registry number, and it became SLU-PP-332 in 2023 when a group at Saint Louis University and collaborating institutions designed it from an earlier molecule, GSK4716, a phenolic acylhydrazone that activates the beta and gamma paralogs and, by the 2005 report that introduced the chemotype, not the alpha one. Reaching the alpha receptor was the stated goal, because the genetic evidence pointing at it had no pharmacological tool to go with it. The design change was a single group: a naphthalene in place of an isopropylphenyl.^[2,3,1]

The name causes two kinds of confusion. First, compounds sharing the SLU-PP prefix do not share its behaviour: SLU-PP-915 is a chemically unrelated thiophene boronic acid, and SLU-PP-1072, which comes from the same GSK4716 ancestry as this molecule, is an inverse agonist rather than an agonist. Second, the literature is written in the vocabulary of exercise physiology, and the phrase in the paper titles describes the transcriptional programme the authors were measuring in animals rather than any property of the molecule. What has been established is narrower: the compound raises the transcriptional output of three named receptors in cell assays, with a measured potency order, and that output is attributable to one paralog in one tissue and to another in another.^[17,18,2,19]

The literature is small and concentrated. Roughly ten studies name the compound, applied across skeletal muscle, heart, kidney and whole-animal metabolic models, and most come from one group of collaborating laboratories whose senior authors declare stock in two companies developing agonists of these receptors. The exceptions come from outside: a pilot study in human primary muscle cells from an Italian group, and two sports anti-doping laboratories, in Cologne and at UCLA, which characterised the molecule analytically with doping control in mind. The Cologne group describes compounds of this kind as potentially relevant to sports drug testing programmes; the UCLA group writes that the World Anti-Doping Agency prohibits the use of exercise mimetics and metabolic modulators in sport. Neither sentence is a listing, and this page does not treat them as one: the 2026 Prohibited List names neither this compound nor this receptor family, and the compound is not an approved medicine or a registered trial intervention in any database searched. There is no human in vivo data of any kind. Nothing else in this library shares this target family either, so the entries offered as related share a research area, mitochondrial and metabolic biology, rather than a target or a chemotype.^{[4,20,21,12,13,22,9,6,10]}

SLU-PP-332 molecular structure

The molecule reads in three parts from one end to the other. A 4-hydroxyphenyl ring carries a carbonyl; the carbonyl is joined through an NH to a nitrogen that is double-bonded to a carbon; and that carbon carries a naphthalene attached at its 2 position. The middle three atoms, C(=O)NH-N=CH, are the acylhydrazone, formed in synthesis by condensing an acyl hydrazide with an aldehyde. Because the central link is a carbon-nitrogen double bond, the molecule has two possible geometries at that bond, and both the database record and every published name specify the E isomer. There are no stereocentres at all.^[1,5]

Each of the three parts has been probed by substitution. Replacing the carbonyl with a sulfonyl abolished activity across a whole analogue series, which the authors attribute to geometry rather than to one lost contact. Replacing the phenol with a pyridine was mostly detrimental but survivable when other parts compensated. The naphthalene is the part the selectivity is pinned on: it was added to reach Phe328 in the alpha paralog, where the other two have an alanine, and the test of that idea is the analogue in which it was swapped for a 3,4-dichlorophenyl group at almost identical computed lipophilicity, polar surface area and acidity. That analogue lost the alpha preference, which is reasonably direct evidence that an extended aromatic surface and not bulk physical properties is doing the work.^[5,2]

The measured and computed properties, gathered in one place rather than left across three sections. Kinetic aqueous solubility of 0.2 micromolar at a computed cLogP of 4.05; a half-life of 31.3 minutes in human liver microsomes with intrinsic clearance of 22 microlitres per minute per milligram, against an earlier report from the same programme placing the half-life at or above 60 minutes in both human and mouse microsomes; ligand efficiencies of 0.42 at the alpha paralog and 0.31 at the gamma; a computed topological polar surface area of 61.7 square angstroms and a computed partition coefficient of 3.7 in the database record, beside the 4.05 the medicinal chemistry paper computed. The protonated molecule is observed at m/z 291.1142 with a dominant product ion at m/z 121.0288. Three things are not measured anywhere that was read: a partition coefficient or acid dissociation constant on material rather than in silico, the isomeric composition and aqueous stability of the hydrazone, and any solid form, salt, hydrate or polymorph. The solubility figure also sits two orders of magnitude below the concentrations much of the cell work uses, which no source read addresses.^[5,12,17,1]

The three-dimensional view on this page is a calculated conformer from PubChem. It is not a measurement, not a bound pose, and not evidence about which accessible geometry a receptor selects. No experimental structure of this molecule exists, and the published pictures of it in a pocket are docking poses and simulation snapshots computed in a crystal structure of the alpha paralog that was solved with a chemically unrelated agonist in it. The one experimental structure in this story is of the parent compound GSK4716 in the gamma paralog's ligand-binding domain, at 2.6 angstroms, in which the phenol hydrogen bonds to Asp328 and the ring on the far side of the hydrazone stacks against Tyr326. Its authors describe the pocket accommodating the ligand through an unexpected rearrangement of the phenol-binding residues, and report that activation by this ligand does not involve the major rearrangement or stabilisation of the C-terminal helix that the conventional account of nuclear receptor activation turns on. Everything structural said here is read across from that.^{[1,5,23,17,24,25]}

There are no stereocentres and no D or L question: every ring is flat and every substituted carbon is aromatic or part of the double bond. What the molecule does have is geometric isomerism at the carbon-nitrogen double bond of the hydrazone, and the database record and the published names both specify the E configuration. No study read here reported a measurement of the E to Z composition of a sample, or of how the hydrazone behaves in solution over time, which for this class of linker is the obvious question and is unaddressed.^[1]

What studies on SLU-PP-332 show

Each card names the experimental system and what was measured. A result in one system is not evidence about another.

What is established about how SLU-PP-332 acts on the three estrogen-related receptors

The receptors this compound acts on are already working before it arrives. The 2004 crystal structure of the alpha paralog's ligand-binding domain bound to a fragment of the coactivator PGC-1alpha, with no ligand present, is the evidence for the constitutive, ligand-independent activity the family is known for, and a later mouse study showed that all three paralogs activate a target promoter in a cell assay only when the coactivator is supplied with them. So an agonist here is a molecule that raises an output that is already running and that depends on a partner protein, rather than one that switches a receptor on.^[15,26]

Where it binds is argued by analogy rather than shown. The parent chemotype's crystal structure in the gamma paralog places that ligand in the ligand-binding pocket of the domain, its phenol hydrogen-bonded to Asp328 and its other aromatic ring stacked on Tyr326, with the pocket's phenol-binding residues rearranged to take it. This compound's design rests on extending that ring to reach Phe328, which the alpha paralog has and the other two replace with alanine. Two results make the idea more than a drawing: the potency shift against the parent compound at the alpha receptor, and the analogue that loses alpha preference when the naphthalene is replaced by a group of matched physicochemical properties. Neither is a structure.^[23,17,2,5]

What follows downstream has been measured as transcription of known target genes: Pdk4 in a muscle cell line, Ddit4 and Slc25a25 transiently in primary myocytes where the response requires the alpha paralog, and TFEB, reported as a direct target gene, in neonatal rat ventricular myocytes and in C2C12 mouse myoblasts. In that same muscle cell line maximal mitochondrial respiration and mitochondrial staining were also higher than in vehicle-treated cells, which is a functional rather than a transcriptional endpoint and carries no test of receptor dependence. The strongest evidence that this is receptor-driven rather than a scaffold artefact does not come from this molecule alone: two chemically unrelated agonists produced the same transcriptional direction in the cardiac study, where genetic dependency experiments attributed the response mainly to the gamma paralog. Taken with the alpha dependence found in skeletal muscle, the honest statement is that the compound raises the activity of a receptor family and cannot distinguish its members.^[2,27,19]

What is still unknown about SLU-PP-332

There is no experimental structure, and that is the largest gap. Nobody has crystallised or imaged this molecule, alone or in a receptor, so every statement about its contacts is a docking or simulation result, and the only alpha-paralog structure available for that modelling was solved with an unrelated agonist in the pocket. For a compound whose design argument is one aromatic ring reaching one phenylalanine, that argument rests on potency shifts and substitution tests rather than on seeing it.^[5,25,23]

Three published potency sets exist for this one compound and they do not agree. The originating paper's cotransfection reporter in HEK293 cells gave 98 nM at the alpha paralog, 230 nM at the beta and 430 nM at the gamma. The thiophene-series paper from the same programme, which used this compound as its reference in a cell-based cotransfection assay, reports 230 nM at the beta paralog and 428 nM at the gamma, which sits with the originating figures. The 2026 structure-activity paper, again from an overlapping group, reports 0.22 micromolar at the alpha paralog and 0.59 micromolar at the gamma, roughly twofold weaker, and no paper acknowledges the difference. No independently curated bioactivity record was retrieved to break the tie. The same pattern appears in the metabolic properties: one paper reports the compound stable in human and mouse microsomes with a half-life at or above 60 minutes, another measures 31.3 minutes in human microsomes. Both discrepancies are probably assay-to-assay, which is the point: nothing in this literature has been replicated between unrelated laboratories, because almost all of it comes from one.^[2,17,5]

No affinity has ever been measured. Binding rests on a protease-protection result on one domain and a thermal shift on another, both qualitative, and the authors record that neither assay worked for both receptors, so the two were never compared in one format. There is also a mismatch between the concentrations used and the measured kinetic solubility of 0.2 micromolar: much of the cell work uses 10 micromolar, fifty times that figure, and what is in solution at that nominal concentration is not addressed by any source read.^[2,5]

The chemistry of the linker is unexamined. An acylhydrazone has a configurable double bond and a hydrolysable bond beside it, and the E configuration on this page comes from a database record and from compound names rather than from a measurement on material: no source reports the isomeric composition of a sample or the stability of the hydrazone in aqueous buffer. The two anti-doping laboratories that mapped in vitro metabolism found different inventories, nine metabolites against 22, on different liver preparations, and both describe their structural assignments as approximate without synthesis.^[1,12,13]

Key papers on SLU-PP-332

1. Synthetic ERRα/β/γ Agonist Induces an ERRα-Dependent Acute Aerobic Exercise Response and Enhances Exercise Capacity.

   Billon C, Sitaula S, Banerjee S, Welch R, Elgendy B, Hegazy L, Oh TG, Kazantzis M, Chatterjee A, Chrivia J, Hayes ME, Xu W, Hamilton A, Huss JM, Zhang L, Walker JK, Downes M, Evans RM, Burris TP (2023), ACS Chemical Biology · Receptor pharmacology with genetic dependency

   The originating paper and the place to begin. It contains the design rationale from GSK4716, the potency set at all three receptors, both biochemical engagement assays, and the knockout-myocyte experiment that is the only clean attribution of a transcriptional response to one paralog.

2. Chemical optimization of the exercise mimetic SLU-PP-332 enables insight into estrogen-related receptor signaling.

   Okda HE, Zhao P, Hayes M, Duvall C, Quillin E, Fang H, Mohammed BM, Hegazy L, Burris TP, Elgendy B (2026), International Journal of Biological Macromolecules · Structure-activity relationship with docking and molecular dynamics

   The most chemically informative source. Read it for what each part of the molecule does: the sulfonyl substitution that kills activity, the matched-property swap that removes paralog preference, and the solubility and clearance figures. Read the modelling as modelling.

3. X-ray crystal structures of the estrogen-related receptor-gamma ligand binding domain in three functional states reveal the molecular basis of small molecule regulation.

   Wang L, Zuercher WJ, Consler TG, Lambert MH, Miller AB, Orband-Miller LA, McKee DD, Willson TM, Nolte RT (2006), The Journal of Biological Chemistry · X-ray crystallography

   The only agonist-bound crystal structure in this receptor family, and the structural foundation every account of this chemotype is built on. It is a different ligand in a different paralog, which is exactly why it is worth reading directly rather than through the citations.

4. In Vitro Metabolism and Analytical Characterization of SLU-PP-332 and SLU-PP-915: Novel Pan-ERR Agonists With Doping Potential.

   Möller T, Krug O, Thevis M (2026), Rapid Communications in Mass Spectrometry · High-resolution mass spectrometry and in vitro metabolism

   An independent characterisation from a laboratory with no stake in the pharmacology, including the fragmentation that confirms the connectivity and the in vitro metabolite map. The clearest view of the molecule as a molecule.

5. Novel Pan-ERR Agonists Ameliorate Heart Failure Through Enhancing Cardiac Fatty Acid Metabolism and Mitochondrial Function.

   Xu W, Billon C, Li H, Wilderman A, Qi L, Graves A, Rideb JRDC, Zhao Y, Hayes M, Yu K, Losby M, Hampton CS, Adeyemi CM, Hong SJ, Nasiotis E, Fu C, Oh TG, Fan W, Downes M, Welch RD, Evans RM, Milosavljevic A, Walker JK, Jensen BC, Pei L, Burris T, Zhang L (2024), Circulation · Animal model with multi-omics and genetic dependency

   The strongest argument in this literature that the readouts are receptor-driven: two chemically unrelated agonists producing the same transcriptional direction, with genetic dependency work pointing at the gamma paralog where the muscle work pointed at the alpha.

6. Targeting ERRs to counteract age-related muscle atrophy associated with physical inactivity: a pilot study.

   Bonanni R, Falvino A, Matticari A, Rinaldi AM, D'Arcangelo G, Cifelli P, Iundusi R, Gasbarra E, Tancredi V, Cariati I, Tarantino U (2025), Frontiers in Physiology · Human primary cell pilot study

   The only human-cell measurement, and a useful lesson in reading it carefully: a wide panel of endpoints in primary myoblasts from twenty donors, with no control that would show the receptor family was involved.

7. Pharmacology of estrogen-related receptors (ERRs) agonists.

   Radwan MO, Guin S, Burris TP (2026), RSC Chemical Biology · Review

   A short current review of the receptor family and its agonists for background on constitutive activity, the three paralogs and their tissue distribution. Written by the originating laboratory, so read it for framing rather than for assessment.

References

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18. 18.Schoepke E, Billon C, Haynes KM, Avdagic A, Sitaula S, Sanders R, Adeyemi CM, Walker JK, Burris TP. (2020). A Selective ERRα/γ Inverse Agonist, SLU-PP-1072, Inhibits the Warburg Effect and Induces Apoptosis in Prostate Cancer Cells. ACS Chemical Biology. 15:2338-2345. doi:10.1021/acschembio.0c00670 · abstract only
19. 19.Xu W, Billon C, Li H, Wilderman A, Qi L, Graves A, Rideb JRDC, Zhao Y, Hayes M, Yu K, Losby M, Hampton CS, Adeyemi CM, Hong SJ, Nasiotis E, Fu C, Oh TG, Fan W, Downes M, Welch RD, Evans RM, Milosavljevic A, Walker JK, Jensen BC, Pei L, Burris T, Zhang L. (2024). Novel Pan-ERR Agonists Ameliorate Heart Failure Through Enhancing Cardiac Fatty Acid Metabolism and Mitochondrial Function. Circulation. 149:227-250. doi:10.1161/CIRCULATIONAHA.123.066542 · full text read
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30. 30.UniProt Consortium. UniProtKB P11474 (ERR1_HUMAN), steroid hormone receptor ERR1, gene ESRRA. UniProtKB. source · database record
31. 31.UniProt Consortium. UniProtKB P62508 (ERR3_HUMAN), estrogen-related receptor gamma, gene ESRRG. UniProtKB. source · database record
32. 32.UniProt Consortium. UniProtKB O95718 (ERR2_HUMAN), steroid hormone receptor ERR2, gene ESRRB. UniProtKB. source · database record